Literature DB >> 6541222

Decoration with myosin subfragment-1 disrupts contacts between microfilaments and the cell membrane in isolated Dictyostelium cortices.

H Bennett, J Condeelis.   

Abstract

We used isolated cortices from ameboid cells of Dictyostelium discoideum to examine the structural nature of attachments between microfilaments and the cell membrane and to determine the effect of myosin subfragment-1 (S-1) on such contacts. By varying several parameters in our previously described isolation procedure (Condeelis, J., 1979. J. Cell Biol., 80:751-758), we have improved this procedure and have been able to isolate stable cortices. In this paper we identify two types of contact sites between microfilaments and the cell membrane similar to those seen in the brush border of intestinal epithelial cells: (a) an end-on attachment between the barbed end of actin filaments and the cell membrane; and (b) a lateral attachment mediated by rod-shaped bridges measuring approximately 6 X 15 nm. The spacing between bridges averages 36 nm, which suggests that the helical twist of the actin filament influences bridge location. Together these contacts account for an average of approximately 25,000 attachments per cell. Incubation of cortices with concentrations of S-1 sufficient to saturate binding sites on the microfilaments caused disruption of the contacts. This observation was confirmed by quantitative morphometry to show a threefold loss in the number of contact sites following S-1 decoration. These results indicate that S-1 decoration should be used with caution when information about the precise location of microfilaments and their attachment to the membrane is required.

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Year:  1984        PMID: 6541222      PMCID: PMC2113297          DOI: 10.1083/jcb.99.4.1434

Source DB:  PubMed          Journal:  J Cell Biol        ISSN: 0021-9525            Impact factor:   10.539


  21 in total

1.  Electron microscopic identification of actin associated with isolated amoeba plasma membranes.

Authors:  T D Pollard; E D Korn
Journal:  J Biol Chem       Date:  1973-01-25       Impact factor: 5.157

2.  Substructure of the myosin molecule. IV. Interactions of myosin and its subfragments with adenosine triphosphate and F-actin.

Authors:  S S Margossian; S Lowey
Journal:  J Mol Biol       Date:  1973-03-05       Impact factor: 5.469

3.  Interaction of phalloidin with actin.

Authors:  A M Lengsfeld; I Löw; T Wieland; P Dancker; W Hasselbach
Journal:  Proc Natl Acad Sci U S A       Date:  1974-07       Impact factor: 11.205

4.  Formation of arrowhead complexes with heavy meromyosin in a variety of cell types.

Authors:  H Ishikawa; R Bischoff; H Holtzer
Journal:  J Cell Biol       Date:  1969-11       Impact factor: 10.539

5.  Ligand-induced movement of lymphocyte membrane macromolecules. II. Mapping of surface moieties.

Authors:  M J Karnovsky; E R Unanue; M Leventhal
Journal:  J Exp Med       Date:  1972-10-01       Impact factor: 14.307

6.  Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method.

Authors:  D T Woodrum; S A Rich; T D Pollard
Journal:  J Cell Biol       Date:  1975-10       Impact factor: 10.539

7.  Redistribution of myosin accompanying capping of surface Ig.

Authors:  G F Schreiner; K Fujiwara; T D Pollard; E R Unanue
Journal:  J Exp Med       Date:  1977-05-01       Impact factor: 14.307

8.  Isolation of concanavalin A caps during various stages of formation and their association with actin and myosin.

Authors:  J Condeelis
Journal:  J Cell Biol       Date:  1979-03       Impact factor: 10.539

9.  Organization of an actin filament-membrane complex. Filament polarity and membrane attachment in the microvilli of intestinal epithelial cells.

Authors:  M S Mooseker; L G Tilney
Journal:  J Cell Biol       Date:  1975-12       Impact factor: 10.539

10.  Effects of myosin and heavy meromyosin on actin-related gelation of HeLa cell extracts.

Authors:  R R Weihing
Journal:  J Cell Biol       Date:  1977-10       Impact factor: 10.539

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  7 in total

1.  Quantitative subcellular study of apical pole membranes from chicken oxyntic cells in resting and HCl secretory state.

Authors:  C S Koenig; M Dabiké; M Bronfman
Journal:  J Cell Biol       Date:  1987-12       Impact factor: 10.539

2.  Anchorage of secretion-competent dense granules on the plasma membrane of bovine platelets in the absence of secretory stimulation.

Authors:  T Morimoto; S Ogihara; H Takisawa
Journal:  J Cell Biol       Date:  1990-07       Impact factor: 10.539

3.  F-actin binds to the cytoplasmic surface of ponticulin, a 17-kD integral glycoprotein from Dictyostelium discoideum plasma membranes.

Authors:  L J Wuestehube; E J Luna
Journal:  J Cell Biol       Date:  1987-10       Impact factor: 10.539

4.  Binding and assembly of actin filaments by plasma membranes from Dictyostelium discoideum.

Authors:  M A Schwartz; E J Luna
Journal:  J Cell Biol       Date:  1986-06       Impact factor: 10.539

5.  Ligand-induced changes in the location of actin, myosin, 95K (alpha-actinin), and 120K protein in amebae of Dictyostelium discoideum.

Authors:  J M Carboni; J S Condeelis
Journal:  J Cell Biol       Date:  1985-06       Impact factor: 10.539

6.  How actin binds and assembles onto plasma membranes from Dictyostelium discoideum.

Authors:  M A Schwartz; E J Luna
Journal:  J Cell Biol       Date:  1988-07       Impact factor: 10.539

7.  Dictyostelium discoideum plasma membranes contain an actin-nucleating activity that requires ponticulin, an integral membrane glycoprotein.

Authors:  A Shariff; E J Luna
Journal:  J Cell Biol       Date:  1990-03       Impact factor: 10.539

  7 in total

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